PMID:9140063
| Citation |
Chattoraj, DK, Ghirlando, R, Park, K, Dibbens, JA and Lewis, MS (1996) Dissociation kinetics of RepA dimers: implications for mechanisms of activation of DNA binding by chaperones. Genes Cells 1:189-99 |
|---|---|
| Abstract |
The replication initiator of plasmid P1, RepA, binds DNA as monomer. The binding is stimulated by the chaperones DnaJ, DnaK and GrpE of Escherichia coli. Two models of chaperone action have been proposed. (i) Chaperones dissociate RepA dimers, which are inactive in DNA binding, into active monomers. (ii) The dissociation occurs spontaneously but the monomeric products require the chaperones for refolding into the active form. The latter model was based on the observation that RepA diluted 1000-fold below the K(D) for dimer dissociation, still required the chaperones for DNA binding. |
| Links | |
| Keywords |
Circular Dichroism; DNA Helicases; DNA Replication; DNA-Binding Proteins/metabolism; Dimerization; Light; Molecular Chaperones/metabolism; Plasmids/genetics; Plasmids/metabolism; Protein Binding; Protein Folding; Proteins/metabolism; Repetitive Sequences, Nucleic Acid; Scattering, Radiation; Trans-Activators; Ultracentrifugation |
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